Lactobacillus plantarum amylase acting on crude starch granules. Native isoforms and activity changes after limited proteolysis.

Abstract:

:The microheterogeneous native amylolytic complex secreted by the isolate A6 of Lactobacillus plantarum revealed a selective enzyme specificity loss when submitted to a limited proteolysis under a suboptimum pH condition. A clear electrophoretic profile change toward just one shorter, more acidic, and equally active polypeptide fragment resulted from the pronase E pretreatment. Although the whole enzyme activity remained apparently unaffected for soluble starch, the native parallel activity on intact and non-gelatinized starch granules either from cereals or tubers was dramatically reduced. This phenomenon was more clearly documented by scanning electron microscopy using the easiest accessible native substrate: wheat starch granules. The anion-exchange-purified native enzymes from L. plantarum displayed a different optimum pH curve when compared with the thermotolerant alpha-amylase from Bacillus licheniformis. The alpha-amylases from the lactic-acid-producing A6 isolate presented an electrophoretic profile easily distinguishable from those from B. liqueniformis and B. subtilis species.

authors

Florêncio JA,Eiras-Stofella DR,Soccol CR,Raimbault M,Guyot JP,Fontana JD

doi

10.1385/abab:84-86:1-9:721

subject

Has Abstract

pub_date

2000-04-01 00:00:00

pages

721-30

eissn

0273-2289

issn

1559-0291

journal_volume

84-86

pub_type

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